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J. Biol. Chem., Vol. 279, Issue 26, 26922-26931, June 25, 2004

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The MAM (Meprin/A5-protein/PTPmu) Domain Is a Homophilic Binding Site Promoting the Lateral Dimerization of Receptor-like Protein-tyrosine Phosphatase µ^*

Valeriu B. Cismasiu, Stefan A. Denes, Helmut Reiländer¶, Hartmut Michel¶, and Stefan E. Szedlacsek||

From the Department of Enzymology, Institute of Biochemistry, Spl. Independentei 296, Bucharest 060031, Romania and the ^¶Department of Membrane Biology, Max-Planck Institute for Biophysics, Heinrich-Hoffmann Str. 7, Frankfurt am Main, 60528, Germany

The MAM (meprin/A5-protein/PTPmu) domain is present in numerous proteins with diverse functions. PTPµ belongs to the MAM-containing subclass of protein-tyrosine phosphatases (PTP) able to promote cell-to-cell adhesion. Here we provide experimental evidence that the MAM domain is a homophilic binding site of PTPµ. We demonstrate that the MAM domain forms oligomers in solution and binds to the PTPµ ectodomain at the cell surface. The presence of two disulfide bridges in the MAM molecule was evidenced and their integrity was found to be essential for MAM homophilic interaction. Our data also indicate that PTPµ ectodomain forms oligomers and mediates the cellular adhesion, even in the absence of MAM domain homophilic binding. Reciprocally, MAM is able to interact homophilically in the absence of ectodomain trans binding. The MAM domain therefore contains independent cis and trans interaction sites and we predict that its main role is to promote lateral dimerization of PTPµ at the cell surface. This finding contributes to the understanding of the signal transduction mechanism in MAM-containing PTPs.

Received for publication, December 2, 2003 , and in revised form, March 10, 2004.

^* This work was supported in part by Deutsche Forschung Gemeinschaft, Fonds der Chemischen Industrie, Romanian Academy, and by a short-term EMBO fellowship (to V. B. C.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Albany Medical College, 47 New Scotland Ave., Albany, NY 12208.

^|| To whom correspondence should be addressed: Dept. of Enzymology, Institute of Biochemistry, Spl. Independentei 296, Bucharest 060031, Romania. Tel.: 40-21-2239069; Fax: 40-21-2239068; E-mail: stefan.szedlacsek{at}biochim.ro.

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